Purification and Characterization of Mr 43,000 Protein Similar to Mr 25,000 Protein, a Substrate for Protein Ser/Thr Kinases, Identified as a Part of Xenopus laevis Vitellogenin B1

Journal of Protein Chemistry

Volumn 22, Issue 6, 2003, Pages 571-583

  Xi, Jin ^a   Sugimoto, Isamu ^a   Yoshitome, Satoshi ^a   Yasuda, Hiroko ^a   Ogura, Kumiko ^a   Mori, Nobuhiro ^b,d   Li, Zhijun ^c   Ito, Susumu ^c   Hashimoto, Eikichi ^a  

^a TOTTORI UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

^c JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

^d United Graduate School of Agr Sci   (Japan)

Author keywords

Amino acid sequence; Phosphorylated protein; Protein processing; Vitellogenin; Xenopus laevis

Indexed keywords

ACID PHOSPHATASE; BINDING PROTEIN; PHOSPHOPROTEIN; PNIXA PROTEIN; PROTEIN P25; PROTEIN P43; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; VITELLOGENIN; VITELLOGENIN B1; ANTIBODY; CHYMOTRYPSIN; CHYMOTRYPSIN A; ESTRADIOL; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ARTICLE; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; MOLECULAR WEIGHT; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; XENOPUS LAEVIS; ANIMAL; CHEMISTRY; CROSS REACTION; DRUG EFFECT; ENZYME SPECIFICITY; FEMALE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOLOGY; ISOLATION AND PURIFICATION; LIVER; MALE; METABOLISM; OOCYTE; OVARY; PH; PRENATAL DEVELOPMENT;

XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHYMOTRYPSIN; CROSS REACTIONS; EMBRYONIC AND FETAL DEVELOPMENT; ESTRADIOL; FEMALE; HYDROGEN-ION CONCENTRATION; LIVER; MALE; MOLECULAR WEIGHT; OOCYTES; OVARY; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN-SERINE-THREONINE KINASES; SUBSTRATE SPECIFICITY; VITELLOGENINS; XENOPUS LAEVIS;

EID: 0347479263     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOPC.0000005507.70216.c8     Document Type: Article

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